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Volumn 7, Issue 3, 1996, Pages 321-328

Structure and function of dynactin

Author keywords

Cytoplasmic dynein; Dynactin; Microtubules; Motility

Indexed keywords


EID: 0001147917     PISSN: 10849521     EISSN: None     Source Type: Journal    
DOI: 10.1006/scdb.1996.0041     Document Type: Article
Times cited : (49)

References (51)
  • 1
    • 0023663075 scopus 로고
    • Identification of a microtubule-based cytoplasmic motor in the nematode C. elegans
    • Lye RJ, Porter ME, Scholey JM, McIntosh JR (1987) Identification of a microtubule-based cytoplasmic motor in the nematode C. elegans. Cell 51:309-318
    • (1987) Cell , vol.51 , pp. 309-318
    • Lye, R.J.1    Porter, M.E.2    Scholey, J.M.3    McIntosh, J.R.4
  • 2
    • 0023608935 scopus 로고
    • MAP 1C is a microtubule-activated ATPase which translocates microtubules in vitro and has dynein-like properties
    • Paschal BM, Shpetner HS, Vallee RB (1987) MAP 1C is a microtubule-activated ATPase which translocates microtubules in vitro and has dynein-like properties. J Cell Biol 105:1273-1282
    • (1987) J Cell Biol , vol.105 , pp. 1273-1282
    • Paschal, B.M.1    Shpetner, H.S.2    Vallee, R.B.3
  • 3
    • 0006163872 scopus 로고
    • Dynein is the motor for retrograde axonal transport of organelles
    • Schnapp BJ, Reese TS (1989) Dynein is the motor for retrograde axonal transport of organelles. Proc Natl Acad Sci USA 86:1548-1552
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 1548-1552
    • Schnapp, B.J.1    Reese, T.S.2
  • 4
    • 0024604298 scopus 로고
    • Cytoplasmic dynein is a minus-end directed motor for membranous organelles
    • Schroer TA, Steuer ER, Sheetz MP (1989) Cytoplasmic dynein is a minus-end directed motor for membranous organelles. Cell 56:937-946
    • (1989) Cell , vol.56 , pp. 937-946
    • Schroer, T.A.1    Steuer, E.R.2    Sheetz, M.P.3
  • 6
    • 0025320820 scopus 로고
    • Localization of cytoplasmic dynein to mitotic spindles and kinetochores
    • Steuer ER, Schroer TA, Wordeman L, Sheetz MP (1990) Localization of cytoplasmic dynein to mitotic spindles and kinetochores. Nature 345:266-268
    • (1990) Nature , vol.345 , pp. 266-268
    • Steuer, E.R.1    Schroer, T.A.2    Wordeman, L.3    Sheetz, M.P.4
  • 7
    • 0025866858 scopus 로고
    • Chemical subdomains within the kinetochore domain of isolated CHO mitotic chromosomes
    • Wordeman L, Steuer E, Sheetz MP, Mitchison TJ (1991) Chemical subdomains within the kinetochore domain of isolated CHO mitotic chromosomes. J Cell Biol 114:285-294
    • (1991) J Cell Biol , vol.114 , pp. 285-294
    • Wordeman, L.1    Steuer, E.2    Sheetz, M.P.3    Mitchison, T.J.4
  • 8
    • 0025789647 scopus 로고
    • Two activators of microtubule-based vesicle transport
    • Schroer TA, Sheetz MP (1991) Two activators of microtubule-based vesicle transport. J Cell Biol 115:1309-1318
    • (1991) J Cell Biol , vol.115 , pp. 1309-1318
    • Schroer, T.A.1    Sheetz, M.P.2
  • 9
    • 0028304474 scopus 로고
    • Ultrastructural analysis of the dynactin complex: An actin-related protein is a component of a filament that resembles f-actin
    • Schafer DA, Gill SR, Cooper JA, Heuser JE, Schroer TA (1994) Ultrastructural analysis of the dynactin complex: An actin-related protein is a component of a filament that resembles f-actin. J Cell Biol 126:403-412
    • (1994) J Cell Biol , vol.126 , pp. 403-412
    • Schafer, D.A.1    Gill, S.R.2    Cooper, J.A.3    Heuser, J.E.4    Schroer, T.A.5
  • 10
    • 0026686929 scopus 로고
    • Centractin is an actin homologue associated with the centrosome
    • Clark SW, Meyer DI (1992) Centractin is an actin homologue associated with the centrosome. Nature 359:246-250
    • (1992) Nature , vol.359 , pp. 246-250
    • Clark, S.W.1    Meyer, D.I.2
  • 11
    • 0026783380 scopus 로고
    • A vertebrate actin-related protein is a component of a multisubunit complex involved in microtubule-based vesicle motility
    • Lees-Miller JP, Helfman DM, Schroer TA (1992) A vertebrate actin-related protein is a component of a multisubunit complex involved in microtubule-based vesicle motility. Nature 359:244-246
    • (1992) Nature , vol.359 , pp. 244-246
    • Lees-Miller, J.P.1    Helfman, D.M.2    Schroer, T.A.3
  • 13
    • 0028670191 scopus 로고
    • Beta-centractin: Characterization and distribution of a new member of the centractin family of actin-related proteins
    • Clark SW, Staub O, Clark IB, Holzbaur EL, Paschal BM, Vallee RB, Meyer DI (1994) Beta-centractin: characterization and distribution of a new member of the centractin family of actin-related proteins. Mol Biol Cell 5:1301-1310
    • (1994) Mol Biol Cell , vol.5 , pp. 1301-1310
    • Clark, S.W.1    Staub, O.2    Clark, I.B.3    Holzbaur, E.L.4    Paschal, B.M.5    Vallee, R.B.6    Meyer, D.I.7
  • 14
  • 15
    • 0027293897 scopus 로고
    • Chaperonin-mediated folding of vertebrate actin-related protein and γ-tubulin
    • Melki R, Vainberg IE, Chow RL, Cowan NJ (1993) Chaperonin-mediated folding of vertebrate actin-related protein and γ-tubulin. J Cell Biol 122:1301-1310
    • (1993) J Cell Biol , vol.122 , pp. 1301-1310
    • Melki, R.1    Vainberg, I.E.2    Chow, R.L.3    Cowan, N.J.4
  • 16
    • 0026345013 scopus 로고
    • Dynactin, a conserved, ubiquitously expressed component of an activator of vesicle motility mediated by cytoplasmic dynein
    • Gill SR, Schroer TA, Szilak I, Steuer ER, Sheetz MP, Cleveland DW (1991) Dynactin, a conserved, ubiquitously expressed component of an activator of vesicle motility mediated by cytoplasmic dynein. J Cell Biol 115:1639-1650
    • (1991) J Cell Biol , vol.115 , pp. 1639-1650
    • Gill, S.R.1    Schroer, T.A.2    Szilak, I.3    Steuer, E.R.4    Sheetz, M.P.5    Cleveland, D.W.6
  • 18
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas A, van Dyke M, Stock J (1991) Predicting coiled coils from protein sequences. Science 252:1162-1164
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3
  • 19
    • 0028986631 scopus 로고
    • The p150Glued component of the dynactin complex binds to both microtubules and the actin-related protein centractin (Arp-1)
    • Waterman-Storer CM, Karki S, Holzbaur ELF (1995) The p150Glued component of the dynactin complex binds to both microtubules and the actin-related protein centractin (Arp-1). Proc Natl Acad Sci USA 92:1634-1638
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 1634-1638
    • Waterman-Storer, C.M.1    Karki, S.2    Holzbaur, E.L.F.3
  • 20
    • 0025597940 scopus 로고
    • BIK1, a protein required for microtubule function during mating and mitosis in Saccharomyces cerevisiae, colocalizes with tubulin
    • Berlin V, Styles CA, Fink GR (1990) BIK1, a protein required for microtubule function during mating and mitosis in Saccharomyces cerevisiae, colocalizes with tubulin. J Cell Biol 111:2573-2586
    • (1990) J Cell Biol , vol.111 , pp. 2573-2586
    • Berlin, V.1    Styles, C.A.2    Fink, G.R.3
  • 21
    • 0026793891 scopus 로고
    • CLIP-170 links endocytic vesicles to microtubules
    • Pierre P, Scheel J, Rickard J, Kreis TE (1992) CLIP-170 links endocytic vesicles to microtubules. Cell 70:887-900
    • (1992) Cell , vol.70 , pp. 887-900
    • Pierre, P.1    Scheel, J.2    Rickard, J.3    Kreis, T.E.4
  • 22
    • 0028806377 scopus 로고
    • Affinity chromatography demonstrates a direct binding between cytoplasmic dynein and the dynactin complex
    • Karki S, Holzbaur ELF (1995) Affinity chromatography demonstrates a direct binding between cytoplasmic dynein and the dynactin complex. J Biol Chem 270:28806-28811
    • (1995) J Biol Chem , vol.270 , pp. 28806-28811
    • Karki, S.1    Holzbaur, E.L.F.2
  • 24
    • 0026706148 scopus 로고
    • Homology of the 74-kD cytoplasmic dynein subunit with a flagellar dynein polypeptide suggests an intracellular targeting function
    • Paschal BM, Mikami A, Pfister KK, Vallee RB (1992) Homology of the 74-kD cytoplasmic dynein subunit with a flagellar dynein polypeptide suggests an intracellular targeting function. J Cell Biol 118:1133-1143
    • (1992) J Cell Biol , vol.118 , pp. 1133-1143
    • Paschal, B.M.1    Mikami, A.2    Pfister, K.K.3    Vallee, R.B.4
  • 26
    • 0029913484 scopus 로고    scopus 로고
    • Molecular characterization of 50 kD subunit of dynactin reveals function for the complex in chromosome alignment and spindle organization during mitosis
    • in press
    • Echeverri CJ, Paschal BM, Vaughan KT, Vallee RB (1996) Molecular characterization of 50 kD subunit of dynactin reveals function for the complex in chromosome alignment and spindle organization during mitosis. J Cell Biol, in press
    • (1996) J Cell Biol
    • Echeverri, C.J.1    Paschal, B.M.2    Vaughan, K.T.3    Vallee, R.B.4
  • 27
    • 0028146484 scopus 로고
    • New insights into the interaction of cytoplasmic dynein with the actin-related protein, Arp1
    • Schroer TA (1994) New insights into the interaction of cytoplasmic dynein with the actin-related protein, Arp1. J Cell Biol 127:1-4
    • (1994) J Cell Biol , vol.127 , pp. 1-4
    • Schroer, T.A.1
  • 28
    • 0027453547 scopus 로고
    • Disruption of mitotic spindle orientation in a yeast dynein mutant
    • Li Y-Y, Yeh E, Hays T, Bloom K (1993) Disruption of mitotic spindle orientation in a yeast dynein mutant. Proc Natl Acad Sci USA 90:10096-10100
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 10096-10100
    • Li, Y.-Y.1    Yeh, E.2    Hays, T.3    Bloom, K.4
  • 30
    • 0028067033 scopus 로고
    • Cytoplasmic dynein and actin-related protein Arp1 are required for normal nuclear distribution in filamentous fungi
    • Plamann M, Minke PF, Tinsley JH, Bruno KS (1994) Cytoplasmic dynein and actin-related protein Arp1 are required for normal nuclear distribution in filamentous fungi. J Cell Biol 127:139-149
    • (1994) J Cell Biol , vol.127 , pp. 139-149
    • Plamann, M.1    Minke, P.F.2    Tinsley, J.H.3    Bruno, K.S.4
  • 31
    • 0028343929 scopus 로고
    • Cytoplasmic dynein is involved in nuclear migration in Aspergillus nidulans
    • Xiang X, Beckwith SM, Morris NR (1994) Cytoplasmic dynein is involved in nuclear migration in Aspergillus nidulans. Proc Natl Acad Sci USA 91:2100-2104
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 2100-2104
    • Xiang, X.1    Beckwith, S.M.2    Morris, N.R.3
  • 32
    • 0028074840 scopus 로고
    • ACT3: A putative centractin homolog in S. cerevisiae is required for proper orientation of the mitotic spindle
    • Clark SW, Meyer DI (1994) ACT3: A putative centractin homolog in S. cerevisiae is required for proper orientation of the mitotic spindle. J Cell Biol 127:129-138
    • (1994) J Cell Biol , vol.127 , pp. 129-138
    • Clark, S.W.1    Meyer, D.I.2
  • 33
    • 0028025571 scopus 로고
    • A yeast actin-related protein homologous to that found in vertebrate dynactin complex is important for spindle orientation and nuclear migration
    • Muhua L, Karpova TS, Cooper JA (1994) A yeast actin-related protein homologous to that found in vertebrate dynactin complex is important for spindle orientation and nuclear migration. Cell 78:669-679
    • (1994) Cell , vol.78 , pp. 669-679
    • Muhua, L.1    Karpova, T.S.2    Cooper, J.A.3
  • 34
    • 0028199609 scopus 로고
    • The JNM1 gene in the yeast Saccharomyces cerevisiae is required for nuclear migration and spindle orientation during the mitotic cell cycle
    • McMillan JN, Tatchell K (1994) The JNM1 gene in the yeast Saccharomyces cerevisiae is required for nuclear migration and spindle orientation during the mitotic cell cycle. J Cell Biol 125:143-158
    • (1994) J Cell Biol , vol.125 , pp. 143-158
    • McMillan, J.N.1    Tatchell, K.2
  • 35
    • 0028787443 scopus 로고
    • Regulation of cytoplasmic dynein function in vivo by the Drosophila Glued complex
    • McGrail M, Gepner J, Silvanovich A, Ludmann S, Serr M, Hays TS (1995) Regulation of cytoplasmic dynein function in vivo by the Drosophila Glued complex. J Cell Biol 131:411-425
    • (1995) J Cell Biol , vol.131 , pp. 411-425
    • McGrail, M.1    Gepner, J.2    Silvanovich, A.3    Ludmann, S.4    Serr, M.5    Hays, T.S.6
  • 36
    • 0020826799 scopus 로고
    • Analysis of visual system development in Drosophila melanogaster. Mutations at the glued locus
    • Harte PJ, Kankel DR (1983) Analysis of visual system development in Drosophila melanogaster. Mutations at the glued locus. Dev Biol 99:88-102
    • (1983) Dev Biol , vol.99 , pp. 88-102
    • Harte, P.J.1    Kankel, D.R.2
  • 38
    • 0039472534 scopus 로고
    • Overexpression of the p50 subunit of dynactin perturbs the positioning of the Golgi apparatus and endosomes
    • Burkhardt JK, Echeverri CJ, Vallee RB (1995) Overexpression of the p50 subunit of dynactin perturbs the positioning of the Golgi apparatus and endosomes. Mol Biol Cell 6:266a
    • (1995) Mol Biol Cell , vol.6
    • Burkhardt, J.K.1    Echeverri, C.J.2    Vallee, R.B.3
  • 39
    • 0026760941 scopus 로고
    • Cytoplasmic dynein participates in centrosomal localization of the Golgi complex
    • Corthesy-Theulaz I, Pauloin A, Pfeffer SR (1992) Cytoplasmic dynein participates in centrosomal localization of the Golgi complex. J Cell Biol 118:1333-1345
    • (1992) J Cell Biol , vol.118 , pp. 1333-1345
    • Corthesy-Theulaz, I.1    Pauloin, A.2    Pfeffer, S.R.3
  • 40
    • 0027730175 scopus 로고
    • Cytoplasmic dynein-dependent vesicular transport from early to late endosomes
    • Aniento F, Emans N, Griffiths G, Gruenberg J (1993) Cytoplasmic dynein-dependent vesicular transport from early to late endosomes. J Cell Biol 123:1373-1387
    • (1993) J Cell Biol , vol.123 , pp. 1373-1387
    • Aniento, F.1    Emans, N.2    Griffiths, G.3    Gruenberg, J.4
  • 41
    • 0026630055 scopus 로고
    • Cytoplasmic dynein is a vesicle protein
    • Lacey ML, Haimo LT (1992) Cytoplasmic dynein is a vesicle protein. J Biol Chem 267:4793-4798
    • (1992) J Biol Chem , vol.267 , pp. 4793-4798
    • Lacey, M.L.1    Haimo, L.T.2
  • 42
    • 0028238805 scopus 로고
    • Cytoplasmic dynein binds to phospholipid vesicles
    • Lacey ML, Haimo LT (1994) Cytoplasmic dynein binds to phospholipid vesicles. Cell Motil Cytoskel 28:205-212
    • (1994) Cell Motil Cytoskel , vol.28 , pp. 205-212
    • Lacey, M.L.1    Haimo, L.T.2
  • 43
    • 0021182208 scopus 로고
    • Ultrastructure of unit fragments of the skeleton of the human erythrocyte membrane
    • Shen BW, Josephs R, Steck TL (1984) Ultrastructure of unit fragments of the skeleton of the human erythrocyte membrane. J Cell Biol 99:810-821
    • (1984) J Cell Biol , vol.99 , pp. 810-821
    • Shen, B.W.1    Josephs, R.2    Steck, T.L.3
  • 44
    • 0024552276 scopus 로고
    • The spectrin-actin junction of erythrocyte membrane skeletons
    • Bennett V (1989) The spectrin-actin junction of erythrocyte membrane skeletons. Biochim Biophys Acta 988:107-121
    • (1989) Biochim Biophys Acta , vol.988 , pp. 107-121
    • Bennett, V.1
  • 45
    • 0028246498 scopus 로고
    • Immunolocalization of tropomodulin, tropomyosin and actin in spread human erythrocyte skeletons
    • Ursitti JA, Fowler VM (1994) Immunolocalization of tropomodulin, tropomyosin and actin in spread human erythrocyte skeletons. J Cell Sci 107:1633-1639
    • (1994) J Cell Sci , vol.107 , pp. 1633-1639
    • Ursitti, J.A.1    Fowler, V.M.2
  • 46
    • 0023061952 scopus 로고
    • Substructure of sidearms on squid axoplasmic vesicles and microtubules visualized by negative contrast electron microscopy
    • Langford GM, Allen RD, Weiss DG (1987) Substructure of sidearms on squid axoplasmic vesicles and microtubules visualized by negative contrast electron microscopy. Cell Motil Cytoskel 7:20-30
    • (1987) Cell Motil Cytoskel , vol.7 , pp. 20-30
    • Langford, G.M.1    Allen, R.D.2    Weiss, D.G.3
  • 47
    • 0026075806 scopus 로고
    • Binding of pp170 to microtubules is regulated by phosphorylation
    • Rickard JE, Kreis TE (1991) Binding of pp170 to microtubules is regulated by phosphorylation. J Biol Chem 266:17597-17605
    • (1991) J Biol Chem , vol.266 , pp. 17597-17605
    • Rickard, J.E.1    Kreis, T.E.2
  • 48
    • 85029465102 scopus 로고
    • glued is regulated in response to cellular effectors in Rat2 cells
    • glued is regulated in response to cellular effectors in Rat2 cells. Mol Biol Cell 5:287a
    • (1994) Mol Biol Cell , vol.5
    • Farshori, P.1    Holzbaur, E.L.F.2
  • 49
    • 0021095633 scopus 로고
    • Procedure for freeze-drying molecules adsorbed to mica flakes
    • Heuser JE (1983) Procedure for freeze-drying molecules adsorbed to mica flakes. J Mol Biol 169:155-195
    • (1983) J Mol Biol , vol.169 , pp. 155-195
    • Heuser, J.E.1
  • 50
    • 0024416678 scopus 로고
    • Protocol for 3-D visualization of molecules on mica via the quick-freeze, deep-etch technique
    • Heuser J (1989) Protocol for 3-D visualization of molecules on mica via the quick-freeze, deep-etch technique. J Electron Microsc Tech 13:244-263
    • (1989) J Electron Microsc Tech , vol.13 , pp. 244-263
    • Heuser, J.1
  • 51
    • 0024280499 scopus 로고
    • Microtubule-associated protein 1C from brain is a two-headed cytosolic dynein
    • Vallee RB, Wall JS, Paschal BM, Shpetner HS (1988) Microtubule-associated protein 1C from brain is a two-headed cytosolic dynein. Nature 332:561-563
    • (1988) Nature , vol.332 , pp. 561-563
    • Vallee, R.B.1    Wall, J.S.2    Paschal, B.M.3    Shpetner, H.S.4


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